The yeast eIF4E-associated protein Eap1p attenuates GCN4 translation upon TOR-inactivation

Ryu Matsuo, Hiroyuki Kubota, Tohru Obata, Keiji Kito, Kazuhisa Ota, Takanari Kitazono, Setsuro Ibayashi, Takuma Sasaki, Mitsuo Iida, Takashi Ito

研究成果: ジャーナルへの寄稿記事

17 引用 (Scopus)

抄録

Amino acid-starved yeast activates the eIF2α kinase Gcn2p to suppress general translation and to selectively derepress the transcription factor Gcn4p, which induces various biosynthetic genes to elicit general amino acid control (GAAC). Well-fed yeast activates the target of rapamycin (TOR) to stimulate translation via the eIF4F complex. A crosstalk was demonstrated between the pathways for GAAC and TOR signaling: the TOR-specific inhibitor rapamycin activates Gcn2p. Here we demonstrate that, upon TOR-inactivation, the putative TOR-regulated eIF4E-associated protein Eap1p likely functions downstream of Gcn2p to attenuate GCN4 translation via a mechanism independent of eIF4E-binding, thereby constituting another interface between the two pathways.

元の言語英語
ページ(範囲)2433-2438
ページ数6
ジャーナルFEBS Letters
579
発行部数11
DOI
出版物ステータス出版済み - 4 25 2005

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Sirolimus
Yeast
Yeasts
Proteins
Amino Acids
Crosstalk
Transcription Factors
Phosphotransferases
Genes

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

これを引用

The yeast eIF4E-associated protein Eap1p attenuates GCN4 translation upon TOR-inactivation. / Matsuo, Ryu; Kubota, Hiroyuki; Obata, Tohru; Kito, Keiji; Ota, Kazuhisa; Kitazono, Takanari; Ibayashi, Setsuro; Sasaki, Takuma; Iida, Mitsuo; Ito, Takashi.

:: FEBS Letters, 巻 579, 番号 11, 25.04.2005, p. 2433-2438.

研究成果: ジャーナルへの寄稿記事

Matsuo, Ryu ; Kubota, Hiroyuki ; Obata, Tohru ; Kito, Keiji ; Ota, Kazuhisa ; Kitazono, Takanari ; Ibayashi, Setsuro ; Sasaki, Takuma ; Iida, Mitsuo ; Ito, Takashi. / The yeast eIF4E-associated protein Eap1p attenuates GCN4 translation upon TOR-inactivation. :: FEBS Letters. 2005 ; 巻 579, 番号 11. pp. 2433-2438.
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abstract = "Amino acid-starved yeast activates the eIF2α kinase Gcn2p to suppress general translation and to selectively derepress the transcription factor Gcn4p, which induces various biosynthetic genes to elicit general amino acid control (GAAC). Well-fed yeast activates the target of rapamycin (TOR) to stimulate translation via the eIF4F complex. A crosstalk was demonstrated between the pathways for GAAC and TOR signaling: the TOR-specific inhibitor rapamycin activates Gcn2p. Here we demonstrate that, upon TOR-inactivation, the putative TOR-regulated eIF4E-associated protein Eap1p likely functions downstream of Gcn2p to attenuate GCN4 translation via a mechanism independent of eIF4E-binding, thereby constituting another interface between the two pathways.",
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T1 - The yeast eIF4E-associated protein Eap1p attenuates GCN4 translation upon TOR-inactivation

AU - Matsuo, Ryu

AU - Kubota, Hiroyuki

AU - Obata, Tohru

AU - Kito, Keiji

AU - Ota, Kazuhisa

AU - Kitazono, Takanari

AU - Ibayashi, Setsuro

AU - Sasaki, Takuma

AU - Iida, Mitsuo

AU - Ito, Takashi

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AB - Amino acid-starved yeast activates the eIF2α kinase Gcn2p to suppress general translation and to selectively derepress the transcription factor Gcn4p, which induces various biosynthetic genes to elicit general amino acid control (GAAC). Well-fed yeast activates the target of rapamycin (TOR) to stimulate translation via the eIF4F complex. A crosstalk was demonstrated between the pathways for GAAC and TOR signaling: the TOR-specific inhibitor rapamycin activates Gcn2p. Here we demonstrate that, upon TOR-inactivation, the putative TOR-regulated eIF4E-associated protein Eap1p likely functions downstream of Gcn2p to attenuate GCN4 translation via a mechanism independent of eIF4E-binding, thereby constituting another interface between the two pathways.

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